ID A0A1Y2WD32_9PEZI Unreviewed; 245 AA.
AC A0A1Y2WD32;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=M426DRAFT_242311 {ECO:0000313|EMBL:OTB07670.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB07670.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB07670.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB07670.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; KZ111530; OTB07670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WD32; -.
DR STRING; 1001833.A0A1Y2WD32; -.
DR InParanoid; A0A1Y2WD32; -.
DR OrthoDB; 1328078at2759; -.
DR Proteomes; UP000242955; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..106
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 112..245
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 245 AA; 27903 MW; DFE23F9F24255D55 CRC64;
MADKLYISET PDDVKNAKGL HLITQSTPNG QATQILLEEL AETYGTSWTT TLINISTNVQ
KEEWFLRLNP NGRIPVLVDN TQNPPFPVHE TSAQLLYLQS TVDKDSKFGF TDPLEQSELI
QWTFFWHGGG APYQGQVSHF LYVAPEKIDY AITRFRNEVL RVFGVLEIRL SGQYTGEPRE
YLAGKGKGKY TIADIKAWPW IKNHERSSIS KQEVQEQFPH LGKWIERISQ RSGVQKGTGS
KYVQS
//
